High temperature sensitivity is intrinsic to voltage-gated potassium channels
Temperature-sensitive transient receptor potential (TRP) ion channels are members of the large tetrameric cation channels superfamily but are considered to be uniquely sensitive to heat, which has been presumed to be due to the existence of an unidentified temperature-sensing domain. Here we report...
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eLife Sciences Publications, Ltd
2014
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4123715/ |
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pubmed-41237152014-08-22 High temperature sensitivity is intrinsic to voltage-gated potassium channels Yang, Fan Zheng, Jie Biophysics and Structural Biology Temperature-sensitive transient receptor potential (TRP) ion channels are members of the large tetrameric cation channels superfamily but are considered to be uniquely sensitive to heat, which has been presumed to be due to the existence of an unidentified temperature-sensing domain. Here we report that the homologous voltage-gated potassium (Kv) channels also exhibit high temperature sensitivity comparable to that of TRPV1, which is detectable under specific conditions when the voltage sensor is functionally decoupled from the activation gate through either intrinsic mechanisms or mutations. Interestingly, mutations could tune Shaker channel to be either heat-activated or heat-deactivated. Therefore, high temperature sensitivity is intrinsic to both TRP and Kv channels. Our findings suggest important physiological roles of heat-induced variation in Kv channel activities. Mechanistically our findings indicate that temperature-sensing TRP channels may not contain a specialized heat-sensor domain; instead, non-obligatory allosteric gating permits the intrinsic heat sensitivity to drive channel activation, allowing temperature-sensitive TRP channels to function as polymodal nociceptors. eLife Sciences Publications, Ltd 2014-07-16 /pmc/articles/PMC4123715/ /pubmed/25030910 http://dx.doi.org/10.7554/eLife.03255 Text en Copyright © 2014, Yang and Zheng http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Yang, Fan Zheng, Jie |
| spellingShingle |
Yang, Fan Zheng, Jie High temperature sensitivity is intrinsic to voltage-gated potassium channels |
| author_facet |
Yang, Fan Zheng, Jie |
| author_sort |
Yang, Fan |
| title |
High temperature sensitivity is intrinsic to voltage-gated potassium channels |
| title_short |
High temperature sensitivity is intrinsic to voltage-gated potassium channels |
| title_full |
High temperature sensitivity is intrinsic to voltage-gated potassium channels |
| title_fullStr |
High temperature sensitivity is intrinsic to voltage-gated potassium channels |
| title_full_unstemmed |
High temperature sensitivity is intrinsic to voltage-gated potassium channels |
| title_sort |
high temperature sensitivity is intrinsic to voltage-gated potassium channels |
| description |
Temperature-sensitive transient receptor potential (TRP) ion channels are members of the large tetrameric cation channels superfamily but are considered to be uniquely sensitive to heat, which has been presumed to be due to the existence of an unidentified temperature-sensing domain. Here we report that the homologous voltage-gated potassium (Kv) channels also exhibit high temperature sensitivity comparable to that of TRPV1, which is detectable under specific conditions when the voltage sensor is functionally decoupled from the activation gate through either intrinsic mechanisms or mutations. Interestingly, mutations could tune Shaker channel to be either heat-activated or heat-deactivated. Therefore, high temperature sensitivity is intrinsic to both TRP and Kv channels. Our findings suggest important physiological roles of heat-induced variation in Kv channel activities. Mechanistically our findings indicate that temperature-sensing TRP channels may not contain a specialized heat-sensor domain; instead, non-obligatory allosteric gating permits the intrinsic heat sensitivity to drive channel activation, allowing temperature-sensitive TRP channels to function as polymodal nociceptors. |
| publisher |
eLife Sciences Publications, Ltd |
| publishDate |
2014 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4123715/ |
| _version_ |
1613121540243587072 |